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Protein

Inactive glutathione S-transferase D3

Gene

GstD3

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at transcript leveli

Functioni

Has no glutathione S-transferase activity.1 Publication

GO - Molecular functioni

  • glutathione peroxidase activity Source: GO_Central
  • glutathione transferase activity Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transferase

Names & Taxonomyi

Protein namesi
Recommended name:
Inactive glutathione S-transferase D31 Publication
Gene namesi
Name:GstD3Imported
Synonyms:gstD22, GSTD3-3Imported
ORF Names:CG4381Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
ProteomesiUP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0010039. GstD3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 199199Inactive glutathione S-transferase D3PRO_0000185955Add
BLAST

Proteomic databases

PaxDbiQ9VG97.
PRIDEiQ9VG97.

Expressioni

Gene expression databases

BgeeiQ9VG97.
GenevisibleiQ9VG97. DM.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

STRINGi7227.FBpp0082042.

Structurei

3D structure databases

ProteinModelPortaliQ9VG97.
SMRiQ9VG97. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 6464GST N-terminalAdd
BLAST
Domaini70 – 199130GST C-terminalAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni34 – 363Glutathione bindingBy similarity
Regioni48 – 503Glutathione bindingBy similarity

Sequence similaritiesi

Belongs to the GST superfamily. Delta family.1 Publication
Contains 1 GST C-terminal domain.Curated
Contains 1 GST N-terminal domain.Curated

Phylogenomic databases

eggNOGiKOG0867. Eukaryota.
COG0625. LUCA.
GeneTreeiENSGT00540000069741.
InParanoidiQ9VG97.
KOiK00799.
OMAiSHTILRY.
OrthoDBiEOG7V1FRJ.
PhylomeDBiQ9VG97.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9VG97-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVGKALGLEF NKKIINTLKG EQMNPDFIKI NPQHSIPTLV DNGFTIWESR
60 70 80 90 100
AILVYLVEKY GKDDALYPKD IQKQAVINQR LYFDMALMYP TLANYYYKAF
110 120 130 140 150
TTGQFGSEED YKKVQETFDF LNTFLEGQDY VAGDQYTVAD IAILANVSNF
160 170 180 190
DVVGFDISKY PNVARWYDHV KKITPGWEEN WAGALDVKKR IEEKQNAAK
Length:199
Mass (Da):22,907
Last modified:May 1, 2000 - v1
Checksum:i0B4D0EF24ADBBC60
GO

Sequence cautioni

The sequence AAM48379.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAO41561.1.
AY118350 mRNA. Translation: AAM48379.3. Different initiation.
PIRiA46681.
RefSeqiNP_788656.1. NM_176479.2.
UniGeneiDm.13818.

Genome annotation databases

EnsemblMetazoaiFBtr0082570; FBpp0082042; FBgn0010039.
GeneIDi48336.
KEGGidme:Dmel_CG4381.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M97702 Genomic DNA. No translation available.
AE014297 Genomic DNA. Translation: AAO41561.1.
AY118350 mRNA. Translation: AAM48379.3. Different initiation.
PIRiA46681.
RefSeqiNP_788656.1. NM_176479.2.
UniGeneiDm.13818.

3D structure databases

ProteinModelPortaliQ9VG97.
SMRiQ9VG97. Positions 1-189.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi7227.FBpp0082042.

Proteomic databases

PaxDbiQ9VG97.
PRIDEiQ9VG97.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0082570; FBpp0082042; FBgn0010039.
GeneIDi48336.
KEGGidme:Dmel_CG4381.

Organism-specific databases

CTDi48336.
FlyBaseiFBgn0010039. GstD3.

Phylogenomic databases

eggNOGiKOG0867. Eukaryota.
COG0625. LUCA.
GeneTreeiENSGT00540000069741.
InParanoidiQ9VG97.
KOiK00799.
OMAiSHTILRY.
OrthoDBiEOG7V1FRJ.
PhylomeDBiQ9VG97.

Miscellaneous databases

GenomeRNAii48336.
NextBioi839330.
PROiQ9VG97.

Gene expression databases

BgeeiQ9VG97.
GenevisibleiQ9VG97. DM.

Family and domain databases

Gene3Di1.20.1050.10. 1 hit.
3.40.30.10. 1 hit.
InterProiIPR010987. Glutathione-S-Trfase_C-like.
IPR004045. Glutathione_S-Trfase_N.
IPR004046. GST_C.
IPR012336. Thioredoxin-like_fold.
[Graphical view]
PfamiPF00043. GST_C. 1 hit.
PF02798. GST_N. 1 hit.
[Graphical view]
SUPFAMiSSF47616. SSF47616. 1 hit.
SSF52833. SSF52833. 1 hit.
PROSITEiPS50405. GST_CTER. 1 hit.
PS50404. GST_NTER. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The glutathione S-transferase D genes. A divergently organized, intronless gene family in Drosophila melanogaster."
    Toung Y.-P.S., Hsieh T.-S., Tu C.-P.D.
    J. Biol. Chem. 268:9737-9746(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: Berkeley.
    Tissue: Larva and Pupae.
  5. Carlson J.W., Booth B., Frise E., Park S., Wan K.H., Yu C., Celniker S.E.
    Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  6. "A preliminary characterization of the cytosolic glutathione transferase proteome from Drosophila melanogaster."
    Saisawang C., Wongsantichon J., Ketterman A.J.
    Biochem. J. 442:181-190(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: LACK OF ENZYME ACTIVITY.

Entry informationi

Entry nameiGSTD3_DROME
AccessioniPrimary (citable) accession number: Q9VG97
Secondary accession number(s): Q8MT68
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: December 9, 2015
This is version 112 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Caution

In vitro shows no activity towards glutathione. Lacks 16 amino acids at the N-terminus including a glutathione binding site known to be important for catalysis.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.